Structure of the murine lysosomal multienzyme complex core. [PDF]
Sci Adv, 2021 The 3D structure of the complex formed by the enzymes GLB1 and CTSA furthers our understanding of lysosomal storage diseases.
Gorelik A +4 more
europepmc +6 more sources
Controlled Orientation of Active Sites in a Nanostructured Multienzyme Complex. [PDF]
Sci Rep, 2016 Multistep cascade reactions in nature maximize reaction efficiency by co-assembling related enzymes. Such organization facilitates the processing of intermediates by downstream enzymes.
Lim SI +7 more
europepmc +4 more sources
CryoEM reveals oligomeric isomers of a multienzyme complex and assembly mechanics. [PDF]
J Struct Biol X, 2023 AbstractPropionyl-CoA carboxylase (PCC) is a multienzyme complex consisting of up to six α-subunits and six ß-subunits. Belonging to a metabolic pathway converging on the citric acid cycle, it is present in most forms of life and irregularities in its assembly lead to serious illness in humans, known as propionic acidemia. Here, we report the cryogenic
Lee JKJ +5 more
europepmc +5 more sources
Identification of a multienzyme complex for glucose metabolism in living cells. [PDF]
J Biol Chem, 2017 Sequential metabolic enzymes in glucose metabolism have long been hypothesized to form multienzyme complexes that regulate glucose flux in living cells. However, it has been challenging to directly observe these complexes and their functional roles in living systems.
Kohnhorst CL +9 more
europepmc +6 more sources
Lysosomal multienzyme complex: pros and cons of working together. [PDF]
Cell Mol Life Sci, 2014 The ubiquitous distribution of lysosomes and their heterogeneous protein composition reflects the versatility of these organelles in maintaining cell homeostasis and their importance in tissue differentiation and remodeling. In lysosomes, the degradation of complex, macromolecular substrates requires the synergistic action of multiple hydrolases that ...
Bonten EJ, Annunziata I, d'Azzo A.
europepmc +6 more sources
GPCRs regulate the assembly of a multienzyme complex for purine biosynthesis. [PDF]
Nat Chem Biol, 2011 G protein-coupled receptors (GPCRs) transmit exogenous signals to the nucleus, promoting a myriad of biological responses via multiple signaling pathways in both healthy and cancerous cells. However, little is known about the response of cytosolic metabolic pathways to GPCR-mediated signaling.
Verrier F +7 more
europepmc +5 more sources
The Multienzyme Complex Nature of Dehydroepiandrosterone Sulfate Biosynthesis. [PDF]
Int J Mol SciDehydroepiandrosterone (DHEA), a precursor of steroid sex hormones, is synthesized by steroid 17-alpha-hydroxylase/17,20-lyase (CYP17A1) with the participation of microsomal cytochrome b5 (CYB5A) and cytochrome P450 reductase (CPR), followed by sulfation by two cytosolic sulfotransferases, SULT1E1 and SULT2A1, for storage and transport to tissues in ...
Tumilovich A +14 more
europepmc +3 more sources
Standardized Ileal Digestibility of Amino Acids in Hybrid Rye Ground to Two Particle Sizes and Fed With or Without Multienzyme Supplement to Young Growing Pigs. [PDF]
J Anim Physiol Anim Nutr (Berl)ABSTRACT A newly developed hybrid rye with enhanced ergot resistance has potential as an alternative energy source for pigs. An experiment was conducted to evaluate the effects of particle size (PS) and multienzyme supplement (MES) on the apparent total tract digestibility (ATTD) of energy and nutrients and the standardized ileal digestibility (SID) of
Song J +3 more
europepmc +2 more sources
Richard Nelson Perham. 27 April 1937—14 February 2015 [PDF]
, 2018 Richard Nelson Perham, FRS, FMedSci, FRSA, was a British professor of structural biochemistry. He undertook his academic career at the University of Cambridge, holding positions as lecturer, reader, chair and head of the Department of Biochemistry, as ...
Charoy, François +6 more
core +3 more sources
The Molecular Origins of Specificity in the Assembly of a Multienzyme Complex [PDF]
Structure, 2005 The pyruvate dehydrogenase (PDH) multienzyme complex is central to oxidative metabolism. We present the first crystal structure of a complex between pyruvate decarboxylase (E1) and the peripheral subunit binding domain (PSBD) of the dihydrolipoyl acetyltransferase (E2).
René A. W. Frank +4 more
openaire +3 more sources